TAF3_MOUSE
ID TAF3_MOUSE Reviewed; 932 AA.
AC Q5HZG4; Q3U490; Q3UWX2; Q8BIU8; Q99JH4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transcription initiation factor TFIID subunit 3;
DE AltName: Full=140 kDa TATA box-binding protein-associated factor;
DE AltName: Full=TBP-associated factor 3;
DE AltName: Full=Transcription initiation factor TFIID 140 kDa subunit;
DE Short=TAF(II)140;
DE Short=TAF140;
DE Short=TAFII-140;
DE Short=TAFII140;
GN Name=Taf3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TAF10.
RC TISSUE=Embryonic carcinoma;
RX PubMed=11438666; DOI=10.1128/mcb.21.15.5109-5121.2001;
RA Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are
RT novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT PHD finger.";
RL Mol. Cell. Biol. 21:5109-5121(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Egg, and Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TBPL2.
RX PubMed=17704303; DOI=10.1101/gad.1583407;
RA Deato M.D.E., Tjian R.;
RT "Switching of the core transcription machinery during myogenesis.";
RL Genes Dev. 21:2137-2149(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-266, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP STRUCTURE BY NMR OF 857-924 IN COMPLEX WITH H3K4ME3 PEPTIDE.
RX PubMed=18682226; DOI=10.1016/j.str.2008.04.015;
RA van Ingen H., van Schaik F.M., Wienk H., Ballering J., Rehmann H.,
RA Dechesne A.C., Kruijzer J.A., Liskamp R.M., Timmers H.T., Boelens R.;
RT "Structural insight into the recognition of the H3K4me3 mark by the TFIID
RT subunit TAF3.";
RL Structure 16:1245-1256(2008).
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription (By similarity). TFIID recognizes and binds promoters
CC with or without a TATA box via its subunit TBP, a TATA-box-binding
CC protein, and promotes assembly of the pre-initiation complex (PIC) (By
CC similarity). The TFIID complex consists of TBP and TBP-associated
CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7,
CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity). The TFIID
CC complex structure can be divided into 3 modules TFIID-A, TFIID-B, and
CC TFIID-C (By similarity). TAF3 forms the TFIID-A module together with
CC TAF5 and TBP (By similarity). Required in complex with TBPL2 for the
CC differentiation of myoblasts into myocytes (PubMed:17704303). The TAF3-
CC TBPL2 complex replaces TFIID at specific promoters at an early stage in
CC the differentiation process (PubMed:17704303).
CC {ECO:0000250|UniProtKB:Q5VWG9, ECO:0000269|PubMed:17704303}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (By similarity).
CC Interacts with TAF10 via histone fold (PubMed:11438666). Interacts with
CC TAF13, TBP, SAP130 and GCN5L2 (By similarity). Interacts with TBPL2
CC (PubMed:17704303). {ECO:0000250|UniProtKB:Q5VWG9,
CC ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:17704303}.
CC -!- INTERACTION:
CC Q5HZG4; Q6SJ95: Tbpl2; NbExp=3; IntAct=EBI-1561080, EBI-1571412;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17704303}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5HZG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5HZG4-2; Sequence=VSP_019736, VSP_019737;
CC -!- DOMAIN: The PHD-type zinc finger mediates binding to histone H3
CC methyllysine at position 4 (H3K4me3). {ECO:0000269|PubMed:18682226}.
CC -!- SIMILARITY: Belongs to the TAF3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH89030.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ292189; CAC34476.1; -; mRNA.
DR EMBL; AK084574; BAC39218.1; -; mRNA.
DR EMBL; AK136045; BAE22792.1; -; mRNA.
DR EMBL; AK154372; BAE32543.1; -; mRNA.
DR EMBL; BC089030; AAH89030.1; ALT_INIT; mRNA.
DR CCDS; CCDS15675.1; -. [Q5HZG4-1]
DR RefSeq; NP_082024.2; NM_027748.3. [Q5HZG4-1]
DR PDB; 2K16; NMR; -; A=857-924.
DR PDB; 2K17; NMR; -; A=857-924.
DR PDBsum; 2K16; -.
DR PDBsum; 2K17; -.
DR AlphaFoldDB; Q5HZG4; -.
DR BMRB; Q5HZG4; -.
DR SMR; Q5HZG4; -.
DR BioGRID; 229072; 3.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR IntAct; Q5HZG4; 9.
DR STRING; 10090.ENSMUSP00000026888; -.
DR iPTMnet; Q5HZG4; -.
DR PhosphoSitePlus; Q5HZG4; -.
DR EPD; Q5HZG4; -.
DR jPOST; Q5HZG4; -.
DR MaxQB; Q5HZG4; -.
DR PaxDb; Q5HZG4; -.
DR PeptideAtlas; Q5HZG4; -.
DR PRIDE; Q5HZG4; -.
DR ProteomicsDB; 259350; -. [Q5HZG4-1]
DR ProteomicsDB; 259351; -. [Q5HZG4-2]
DR Antibodypedia; 24519; 138 antibodies from 26 providers.
DR Ensembl; ENSMUST00000026888; ENSMUSP00000026888; ENSMUSG00000025782. [Q5HZG4-1]
DR GeneID; 209361; -.
DR KEGG; mmu:209361; -.
DR UCSC; uc008ihk.2; mouse. [Q5HZG4-2]
DR UCSC; uc008ihl.2; mouse. [Q5HZG4-1]
DR CTD; 83860; -.
DR MGI; MGI:2388097; Taf3.
DR VEuPathDB; HostDB:ENSMUSG00000025782; -.
DR eggNOG; KOG1973; Eukaryota.
DR eggNOG; KOG2389; Eukaryota.
DR GeneTree; ENSGT00710000106806; -.
DR HOGENOM; CLU_014486_0_0_1; -.
DR InParanoid; Q5HZG4; -.
DR OMA; FPQPGAR; -.
DR PhylomeDB; Q5HZG4; -.
DR TreeFam; TF316513; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 209361; 22 hits in 79 CRISPR screens.
DR ChiTaRS; Taf3; mouse.
DR EvolutionaryTrace; Q5HZG4; -.
DR PRO; PR:Q5HZG4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5HZG4; protein.
DR Bgee; ENSMUSG00000025782; Expressed in animal zygote and 233 other tissues.
DR ExpressionAtlas; Q5HZG4; baseline and differential.
DR Genevisible; Q5HZG4; MM.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:MGI.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00576; BTP; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..932
FT /note="Transcription initiation factor TFIID subunit 3"
FT /id="PRO_0000245529"
FT ZN_FING 867..917
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 130..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 266
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT MOD_RES 779
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT CROSSLNK 749
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VWG9"
FT VAR_SEQ 1..741
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019736"
FT VAR_SEQ 742..747
FT /note="KHKHEK -> MYKFPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019737"
FT CONFLICT 545
FT /note="R -> G (in Ref. 2; BAE32543)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="K -> E (in Ref. 2; BAE22792)"
FT /evidence="ECO:0000305"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:2K16"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:2K16"
FT STRAND 866..868
FT /evidence="ECO:0007829|PDB:2K16"
FT TURN 871..873
FT /evidence="ECO:0007829|PDB:2K16"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:2K16"
FT STRAND 886..893
FT /evidence="ECO:0007829|PDB:2K16"
FT HELIX 894..897
FT /evidence="ECO:0007829|PDB:2K16"
FT STRAND 905..907
FT /evidence="ECO:0007829|PDB:2K16"
FT TURN 912..914
FT /evidence="ECO:0007829|PDB:2K16"
FT HELIX 915..918
FT /evidence="ECO:0007829|PDB:2K16"
SQ SEQUENCE 932 AA; 105115 MW; 8061D8E599A650EE CRC64;
MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH RYSELYGRTD
PILDDVGEAF QLMGVNLHEL EDYIHNIEPV TFPHQIPSFP VSKNNVLQFP QPGSKDAEER
KDYIPDYLPP IVSSQEEEEE EQVPTDGGTS AEAMQVPLEE DDEMEEEEVI NDENFLGKRP
LDSPEVEEMP SMKRPRLLST KGDSLDVVLL EAREPLSSIN PQKTPPVLSP VRVQDRADLA
PPSPQPPMLA PFAKSQLPIA KPLETKSFTP KTKTKASSPG QKTKSPKAAL SPARLGSPIR
SPKTIPKEKK SPGRSKSPKS PKSPKIVAHV PQTPVRPETP NRTPSAMVVE KTVKETIPVM
KPTQTPPEVV KLNIEMQPKK PVVTDKTIDD SIDAVIARAC AEREPDPFEF SSGSESEGDT
FTSPKRISGS ECATPKASTS SNNFTKSLAT PLPLSSGTSS SDNSWTMDAS IDEVVRKAKL
GAPSNMPPTF PYISSPSISP PTPEPLHKGY EEKAKLPSSV DVKKKLKKEL KTKLKKKEKQ
RDRERERERN KERSKEKDKM REREKEKEAG KELKYPWREL MKDEDSDPYK FKIKEFEDID
AAKVRLKDGI VRREREKHKD KKKDRERSKR EKDKRERERL KEKNREDKIK APPTQLVLPP
KEMALPLFSP SAVRVPAMLP AFSPMLPEKL FEEKEKPKEK ERKKDKKEKK KKKEKEKEKE
KKEREREKER REREKREKEK EKHKHEKIKV EPVIPAPSPV IPRLTLRVGA GQDKIVISKV
VPAPEAKPAP SLNRPKTPPP APVPIPVRVS PTPLQPPLLT QAAVCPALMP SPAPALSGIG
SAKAPVRSVV TETVSTYVIR DEWGNQIWIC PGCNKPDDGS PMIGCDDCDD WYHWPCVGIM
AAPPEEMQWF CPKCANKIKK DKKHKKRKHR AH
